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Crystal structure of aqpz F43W,H174G,T183F
Analyse Crystal structure of aqpz F43W,H174G,T183F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NKC
- Type
- protein
- Length
- 464 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aquaporin Z
- UniProt
- P60844
- Pockets
- 5 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aquaporin Z | protein | 231 | 74% helix, 0% strand | P60844 |
| B | Aquaporin Z | protein | 233 | 73% helix, 0% strand | P60844 |
Ligands and binding sites
- BOG · octyl beta-D-glucopyranoside · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.51 | 0.81 | 27 | empty |
| 2 | 122 | 0.46 | 0.78 | 23 | empty |
| 3 | 106 | 0.41 | 0.77 | 24 | empty |
| 4 | 90 | 0.39 | 0.77 | 24 | empty |
| 5 | 97 | 0.31 | 0.72 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 134 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P60844
- Elsewhere: RCSB PDB 3NKC · PDBe 3NKC · UniProt P60844
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